ID A0A089XC86_STRGA Unreviewed; 533 AA.
AC A0A089XC86;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Polysaccharide lyase {ECO:0000313|EMBL:AIR99526.1};
GN ORFNames=SGLAU_17815 {ECO:0000313|EMBL:AIR99526.1};
OS Streptomyces glaucescens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR99526.1, ECO:0000313|Proteomes:UP000029482};
RN [1] {ECO:0000313|Proteomes:UP000029482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL J. Biotechnol. 194:81-83(2015).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 9 family.
CC {ECO:0000256|ARBA:ARBA00038263}.
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DR EMBL; CP009438; AIR99526.1; -; Genomic_DNA.
DR RefSeq; WP_043502643.1; NZ_CP009438.1.
DR AlphaFoldDB; A0A089XC86; -.
DR STRING; 1907.SGLAU_17815; -.
DR KEGG; sgu:SGLAU_17815; -.
DR eggNOG; COG3266; Bacteria.
DR eggNOG; COG4733; Bacteria.
DR HOGENOM; CLU_034062_0_0_11; -.
DR OrthoDB; 8660908at2; -.
DR Proteomes; UP000029482; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd04082; CBM35_pectate_lyase-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1.
DR PANTHER; PTHR40088:SF1; PECTATE LYASE PEL9; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF03422; CBM_6; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AIR99526.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029482};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..533
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001851598"
FT DOMAIN 37..161
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
SQ SEQUENCE 533 AA; 55204 MW; 2B010A65AE967B18 CRC64;
MHQRRAPRPV LPVIASAGLL AGTLVALSGT TAQAATARYE AETSPAVCTG AIESEWSGYS
GSGFCNATNA TGAYVQFTAS APAAGTATLR IRFANGTTTA RPATLTVNGT AAGSPSFEGT
GAWSTWSTKT LTVSLAAGSN TIRLTPTTSG GLPNIDYLEV ETAGDTTPPP TTGSVLYVAP
NGTDGAAGTQ TSPTTLTSAI SRITPGGTIY VRGGTYSYAQ TVTIPPTNNG TASARTRLTA
YPGERPVLDF SAQPEDPANR GLALNGSYWH VHGLTVQRAG DNGIFIGGSN NVVERTVTRY
NRDTGLQLSR MASTTPASQW PSNNLILSAE SHDNADSDGE DADGFAAKLT SGPGNVFRYA
VAHNNIDDGW DLYTKSDTGP IGAVTIEDSL AYENGTLSDG SQAGAGDRNG YKLGGEDIPV
NHVVRRSIAY DNGKHGFTYN SNPGSMTVSD NVSVDNAQRN FNFDAGTSVF RGNTSCRSGS
GTNDRIIGNA DSTNQFWSGT NGSRCASYSG ALNWSYASDG RLVVTFGGNR VTP
//
